Some like it cold: biocatalysis at low temperatures

• Published in: FEMS microbiology reviews Vol. 28; no. 1; pp. 25 - 42
• Main Authors: Georlette, D., Blaise, V., Collins, T., D’Amico, S., Gratia, E., Hoyoux, A., Marx, J.-C., Sonan, G., Feller, G., Gerday, C.
• Format: Journal Article Web Resource
• Language: English
• Published: Oxford, UK Elsevier B.V 01.02.2004; Elsevier Science Bv; Blackwell Publishing Ltd; Blackwell; Oxford University Press
• Subjects: Action of physical and chemical agents on bacteria; Adaptation, Physiological; Bacterial Physiological Phenomena; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Bacteriology; Biochemistry; Biochemistry, biophysics & molecular biology; Biochimie, biophysique & biologie moléculaire; Biological and medical sciences; biophysics; Biotechnology; Catalysis; Chemical reactions; Cold; Cold Temperature; Cold-adaptation; Crystallography; Enzyme activity; Enzyme kinetics; Enzymes; Enzymes - chemistry; Enzymes - metabolism; Extremophiles; Flexibility concept; Fluxes; Fundamental and applied biological sciences. Psychology; Life sciences; Low temperature; Microbiology; molecular biology; Organic chemistry; Organisms; Protein engineering; Protein structure; Proteins; Psychrophiles; Sciences du vivant; Thermal compensation; Thermal stability; X-ray crystallography; Enzyme activity; Cold-adaptation; Enzyme kinetics; Psychrophiles; Extremophiles; Flexibility concept; Temperature; Enzymatic activity; Enzyme; Psychrophily; Biological model; Bacteria; Kinetics; Adaptation
• ISSN: 0168-6445; 1574-6976; 1574-6976
• DOI: 10.1016/j.femsre.2003.07.003

In the last few years, increased attention has been focused on a class of organisms called psychrophiles. These organisms, hosts of permanently cold habitats, often display metabolic fluxes more or less comparable to those exhibited by mesophilic organisms at moderate temperatures. Psychrophiles have evolved by producing, among other peculiarities, “cold-adapted” enzymes which have the properties to cope with the reduction of chemical reaction rates induced by low temperatures. Thermal compensation in these enzymes is reached, in most cases, through a high catalytic efficiency associated, however, with a low thermal stability. Thanks to recent advances provided by X-ray crystallography, structure modelling, protein engineering and biophysical studies, the adaptation strategies are beginning to be understood. The emerging picture suggests that psychrophilic enzymes are characterized by an improved flexibility of the structural components involved in the catalytic cycle, whereas other protein regions, if not implicated in catalysis, may be even more rigid than their mesophilic counterparts. Due to their attractive properties, i.e., a high specific activity and a low thermal stability, these enzymes constitute a tremendous potential for fundamental research and biotechnological applications.